A tandem mass spectrometric approach to determination of chondroitin/dermatan sulfate oligosaccharide glycoforms
Author
Summary, in English
Dermatan sulfate (DS) chains are variants of chondroitin sulfate (CS) that are expressed in mammalian extracellular matrices and are particularly prevalent in skin. DS has been implicated in varied biological processes including wound repair, infection, cardiovascular disease, tumorigenesis, and fibrosis. The biological activities of DS have been attributed to its high content of IdoA(alpha 1-3)GalNAc4S(beta 1-4) disaccharide units. Mature CS/DS chains consist of blocks with high and low GlcA/IdoA ratios, and sulfation may occur at the 4- and/or 6-position of GalNAc and 2-position of IdoA. Traditional methods for the analysis of CS/DS chains involve differential digestion with specific chondroitinases followed by steps of chromatographic isolation of the products and di-saccharide analysis on the individual fraction. This work reports the use of tandem mass spectrometry to determine the patterns of sulfation and epimerization of CS/DS oligosaccharides in a single step. The approach is first validated and then applied to a series of skin DS samples and to decorins from three different tissues. DS samples ranged from 74 to 99% of CSB-like repeats, using this approach. Decorin samples ranged from 30% CSB-like repeats for those samples from articular cartilage to 75% for those from sclera. These values agree with known levels of glucuronyl C5-epimerase in these tissues.
Department/s
- Matrix Biology
Publishing year
2006
Language
English
Pages
502-513
Publication/Series
Glycobiology
Volume
16
Issue
6
Document type
Journal article
Publisher
Oxford University Press
Topic
- Biochemistry and Molecular Biology
Keywords
- dermatan sulfate
- glycosaminoglycan
- spectrometry
- mass
- decorin
- chondroitin sulfate
Status
Published
Research group
- Matrix Biology
ISBN/ISSN/Other
- ISSN: 1460-2423